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CAZyme Information: MGYG000000325_01595
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-95; | |||||||||||
| CAZyme ID | MGYG000000325_01595 | |||||||||||
| CAZy Family | CE17 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 23236; End: 24363 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| CE17 | 37 | 200 | 4.2e-73 | 0.9939393939393939 |
| CBM35inCE17 | 231 | 374 | 9e-59 | 0.959731543624161 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd00229 | SGNH_hydrolase | 2.06e-22 | 35 | 209 | 1 | 187 | SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the typical Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid. |
| pfam13472 | Lipase_GDSL_2 | 2.55e-17 | 37 | 201 | 1 | 176 | GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657. |
| cd01834 | SGNH_hydrolase_like_2 | 1.86e-13 | 33 | 206 | 2 | 188 | SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases. |
| COG2755 | TesA | 4.82e-11 | 30 | 218 | 3 | 216 | Lysophospholipase L1 or related esterase [Amino acid transport and metabolism]. |
| cd01822 | Lysophospholipase_L1_like | 1.18e-08 | 38 | 211 | 6 | 177 | Lysophospholipase L1-like subgroup of SGNH-hydrolases. The best characterized member in this family is TesA, an E. coli periplasmic protein with thioesterase, esterase, arylesterase, protease and lysophospholipase activity. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| BCN32107.1 | 9.89e-163 | 1 | 374 | 1 | 370 |
| CBL10432.1 | 1.81e-146 | 1 | 375 | 1 | 370 |
| CBL12377.1 | 1.81e-146 | 1 | 375 | 1 | 370 |
| EEV02614.1 | 3.65e-146 | 1 | 375 | 1 | 370 |
| AEN97394.1 | 8.28e-134 | 1 | 374 | 1 | 381 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6HH9_A | 1.64e-147 | 1 | 375 | 1 | 370 | Crystalstructure of a two-domain esterase (CEX) active on acetylated mannans co-crystallized with mannopentaose [Roseburia intestinalis L1-82],6HH9_B Crystal structure of a two-domain esterase (CEX) active on acetylated mannans co-crystallized with mannopentaose [Roseburia intestinalis L1-82],6HH9_C Crystal structure of a two-domain esterase (CEX) active on acetylated mannans co-crystallized with mannopentaose [Roseburia intestinalis L1-82],6HH9_D Crystal structure of a two-domain esterase (CEX) active on acetylated mannans co-crystallized with mannopentaose [Roseburia intestinalis L1-82] |
| 6HFZ_A | 6.23e-145 | 3 | 375 | 3 | 370 | Crystalstructure of a two-domain esterase (CEX) active on acetylated mannans [Roseburia intestinalis L1-82],6HFZ_B Crystal structure of a two-domain esterase (CEX) active on acetylated mannans [Roseburia intestinalis L1-82],6HFZ_C Crystal structure of a two-domain esterase (CEX) active on acetylated mannans [Roseburia intestinalis L1-82],6HFZ_D Crystal structure of a two-domain esterase (CEX) active on acetylated mannans [Roseburia intestinalis L1-82] |
| 5TID_A | 1.10e-07 | 38 | 213 | 10 | 180 | X-raystructure of acyl-CoA thioesterase I, TesA, mutant M141L/Y145K/L146K at pH 5 in complex with octanoic acid [Escherichia coli],5TIE_A x-ray structure of acyl-CoA thioesterase I, TesA, mutant M141L/Y145K/L146K at pH 7.5 in complex with octanoic acid [Escherichia coli],5TIF_A x-ray structure of acyl-CoA thioesterase I, TesA, triple mutant M141L/Y145K/L146K in complex with octanoic acid [Escherichia coli] |
| 1IVN_A | 1.18e-07 | 38 | 220 | 7 | 184 | E.coliThioesterase I/Protease I/Lysophospholiase L1 [Escherichia coli],1U8U_A E. coli Thioesterase I/Protease I/Lysophospholiase L1 in complexed with octanoic acid [Escherichia coli] |
| 5TIC_A | 1.48e-07 | 38 | 213 | 10 | 180 | X-raystructure of wild-type E. coli Acyl-CoA thioesterase I at pH 5 [Escherichia coli],5TIC_B X-ray structure of wild-type E. coli Acyl-CoA thioesterase I at pH 5 [Escherichia coli] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P0ADA1 | 1.10e-06 | 38 | 213 | 33 | 203 | Thioesterase 1/protease 1/lysophospholipase L1 OS=Escherichia coli (strain K12) OX=83333 GN=tesA PE=1 SV=1 |
| P0ADA2 | 1.10e-06 | 38 | 213 | 33 | 203 | Thioesterase 1/protease 1/lysophospholipase L1 OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=tesA PE=3 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000047 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |